E3 ubiquitin-protein ligase arkadia-B (rnf111-b) Recombinant Protein | rnf111-b recombinant protein

Recombinant Xenopus laevis E3 ubiquitin-protein ligase arkadia-B (rnf111-b), partial

• Gene Names: rnf111-b; rnf111; arkadia
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase arkadia-B (rnf111-b); Recombinant Xenopus laevis E3 ubiquitin-protein ligase arkadia-B (rnf111-b); partial; rnf111-b recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 959

• Species: Xenopus laevis (African clawed frog)
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 148234951
• NCBI GeneID: 779113
• NCBI Accession #: NP_001090211.1
• NCBI GenBank Nucleotide #: NM_001096742.1
• UniProt Accession #: Q6NRV8
• Molecular Weight: 105,433 Da
• NCBI Official Full Name: E3 ubiquitin-protein ligase arkadia-B
• NCBI Official Symbol: rnf111-b
• NCBI Official Synonym Symbols: rnf111; arkadia
• NCBI Protein Information: E3 ubiquitin-protein ligase arkadia-B
• UniProt Protein Name: E3 ubiquitin-protein ligase arkadia-B
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: rnf111-b

Uniprot Description

E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development (). Acts as an enhancer of the transcriptional responses of the smad2/smad3 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as smad7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) ().